ID   PLPL_ASPNC              Reviewed;         749 AA.
AC   A2Q8F7;
DT   24-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT   06-MAR-2007, sequence version 1.
DT   25-MAY-2022, entry version 65.
DE   RecName: Full=Patatin-like phospholipase domain-containing protein An01g04180;
DE            EC=3.1.1.-;
GN   ORFNames=An01g04180;
OS   Aspergillus niger (strain CBS 513.88 / FGSC A1513).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Circumdati.
OX   NCBI_TaxID=425011;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 513.88 / FGSC A1513 / ATCC MYA-4892;
RX   PubMed=17259976; DOI=10.1038/nbt1282;
RA   Pel H.J., de Winde J.H., Archer D.B., Dyer P.S., Hofmann G., Schaap P.J.,
RA   Turner G., de Vries R.P., Albang R., Albermann K., Andersen M.R.,
RA   Bendtsen J.D., Benen J.A.E., van den Berg M., Breestraat S., Caddick M.X.,
RA   Contreras R., Cornell M., Coutinho P.M., Danchin E.G.J., Debets A.J.M.,
RA   Dekker P., van Dijck P.W.M., van Dijk A., Dijkhuizen L., Driessen A.J.M.,
RA   d'Enfert C., Geysens S., Goosen C., Groot G.S.P., de Groot P.W.J.,
RA   Guillemette T., Henrissat B., Herweijer M., van den Hombergh J.P.T.W.,
RA   van den Hondel C.A.M.J.J., van der Heijden R.T.J.M., van der Kaaij R.M.,
RA   Klis F.M., Kools H.J., Kubicek C.P., van Kuyk P.A., Lauber J., Lu X.,
RA   van der Maarel M.J.E.C., Meulenberg R., Menke H., Mortimer M.A.,
RA   Nielsen J., Oliver S.G., Olsthoorn M., Pal K., van Peij N.N.M.E.,
RA   Ram A.F.J., Rinas U., Roubos J.A., Sagt C.M.J., Schmoll M., Sun J.,
RA   Ussery D., Varga J., Vervecken W., van de Vondervoort P.J.J., Wedler H.,
RA   Woesten H.A.B., Zeng A.-P., van Ooyen A.J.J., Visser J., Stam H.;
RT   "Genome sequencing and analysis of the versatile cell factory Aspergillus
RT   niger CBS 513.88.";
RL   Nat. Biotechnol. 25:221-231(2007).
CC   -!- FUNCTION: Probable lipid hydrolase. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass membrane
CC       protein {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the PLPL family. {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AM269961; CAK36954.1; -; Genomic_DNA.
DR   RefSeq; XP_001388846.1; XM_001388809.2.
DR   AlphaFoldDB; A2Q8F7; -.
DR   PaxDb; A2Q8F7; -.
DR   EnsemblFungi; CAK36954; CAK36954; An01g04180.
DR   GeneID; 4978123; -.
DR   KEGG; ang:ANI_1_534014; -.
DR   VEuPathDB; FungiDB:An01g04180; -.
DR   HOGENOM; CLU_009031_2_2_1; -.
DR   Proteomes; UP000006706; Chromosome 2R.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005811; C:lipid droplet; IEA:EnsemblFungi.
DR   GO; GO:0004806; F:triglyceride lipase activity; IEA:EnsemblFungi.
DR   GO; GO:1990748; P:cellular detoxification; IEA:EnsemblFungi.
DR   GO; GO:0016042; P:lipid catabolic process; IEA:UniProtKB-KW.
DR   GO; GO:0006642; P:triglyceride mobilization; IEA:EnsemblFungi.
DR   InterPro; IPR016035; Acyl_Trfase/lysoPLipase.
DR   InterPro; IPR002641; PNPLA_dom.
DR   InterPro; IPR021771; Triacylglycerol_lipase_N.
DR   Pfam; PF11815; DUF3336; 1.
DR   Pfam; PF01734; Patatin; 1.
DR   SUPFAM; SSF52151; SSF52151; 1.
DR   PROSITE; PS51635; PNPLA; 1.
PE   3: Inferred from homology;
KW   Hydrolase; Lipid degradation; Lipid metabolism; Membrane;
KW   Reference proteome; Transmembrane; Transmembrane helix.
FT   CHAIN           1..749
FT                   /note="Patatin-like phospholipase domain-containing protein
FT                   An01g04180"
FT                   /id="PRO_0000295551"
FT   TRANSMEM        87..107
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          277..468
FT                   /note="PNPLA"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01161"
FT   REGION          1..21
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          619..726
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           308..312
FT                   /note="GXSXG"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01161"
FT   COMPBIAS        628..646
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        684..707
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        310
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01161"
FT   ACT_SITE        455
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01161"
SQ   SEQUENCE   749 AA;  85597 MW;  18CE7FC9EF7190E6 CRC64;
     MNGAEKSAAG DTYDPSTIPD YDREFIHPDD LRQFELALTD QGASPLVALN DWRPIYQRVR
     RERGRRKEPR RTKDETREGV LYTVLKWPFL FTVFGWITAL AFAYTLTRVY IFLYEQWVTW
     RGRRQSLRRQ LHAQTNYPDW QKAARALDDH LGNQRWKEID EYAYYDHLTI SNLVKQLKKV
     RREVERERRE KRRGSGQSPA AEELCTLLEA CVKNNFAGVE NPRLYSEAYS GTKNLVQEYI
     DELHACIQLV ADSKGITSEE KLQHFKHLDT NFGRTALCLS GGATFAYYHF GVVRALLDNG
     VLPEIITGTS GGALVAALVA TRTDEELKQL LVPALAHRIR ACQESFPTWV WRWWRTGARF
     DTLDWARQCS WFCRGSTTFR EAYERTGRIL NVSCVPSDPH SPTILANYLT SPNCVIWSAV
     LASAAVPGIL NPVVLMTKKR DGTLAPYSFG HKWKDGSLRT DIPIKALNLH FNVNFTIVSQ
     VNPHINLFFF SSRGTVGRPV THRKGRGWRG GFLGSAIEQY IKLDMNKWLR VLRHLELLPR
     PMGQDWSEIW LQKFSGTVTI WPKTIPSDFY HILSDPNPER LARMLRVGQQ SAFPKLQFIK
     NRLKIEIAVV KSLQKFAHAG GRPISPAPSR WRQNNDPDNH YNPSPRTDPL NERLDHNLPE
     RRGDNVNITF GEGGGREDTH LLDGSLSENS SNESAARPSS SSSSSRLLRV PEHRRGSTGS
     SIFEEVRRQS AVFFDDVDMY GDDEALRPG